DC1I2_BOVIN
ID DC1I2_BOVIN Reviewed; 612 AA.
AC Q0III3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2;
DE AltName: Full=Cytoplasmic dynein intermediate chain 2;
DE AltName: Full=Dynein intermediate chain 2, cytosolic;
DE Short=DH IC-2;
GN Name=DYNC1I2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=11967380; DOI=10.1110/ps.2520102;
RA King S.J., Bonilla M., Rodgers M.E., Schroer T.A.;
RT "Subunit organization in cytoplasmic dynein subcomplexes.";
RL Protein Sci. 11:1239-1250(2002).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. The
CC intermediate chains mediate the binding of dynein to dynactin via its
CC 150 kDa component (p150-glued) DCTN1. Involved in membrane-transport,
CC such as Golgi apparatus, late endosomes and lysosomes.
CC {ECO:0000250|UniProtKB:Q62871}.
CC -!- SUBUNIT: Homodimer (PubMed:11967380). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition
CC (PubMed:11967380). The heavy chain homodimer serves as a scaffold for
CC the probable homodimeric assembly of the respective non-catalytic
CC subunits (PubMed:11967380). The ICs and LICs bind directly to the HC
CC dimer and the LCs assemble on the IC dimer (PubMed:11967380). Interacts
CC with DYNLT3. Interacts with DYNLT1. Interacts (dephosphorylated at Ser-
CC 84) with DCTN1 (By similarity). Interacts with BICD2. Interacts with
CC SPEF2 (By similarity). {ECO:0000250|UniProtKB:O88487,
CC ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:11967380}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O88487}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of
CC pachytene spermatocytes. Localizes to the manchette in elongating
CC spermatids. {ECO:0000250|UniProtKB:O88487}.
CC -!- PTM: The phosphorylation status of Ser-84 appears to be involved in
CC dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) promotes interaction with DCTN1. Serine pyrophosphorylation is
CC achieved by Mg(2+)-dependent, but enzyme independent transfer of a
CC beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated
CC serine residue. {ECO:0000250|UniProtKB:O88487}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; BC122627; AAI22628.1; -; mRNA.
DR RefSeq; NP_001069351.1; NM_001075883.1.
DR AlphaFoldDB; Q0III3; -.
DR SMR; Q0III3; -.
DR STRING; 9913.ENSBTAP00000003429; -.
DR PaxDb; Q0III3; -.
DR PeptideAtlas; Q0III3; -.
DR PRIDE; Q0III3; -.
DR GeneID; 526329; -.
DR KEGG; bta:526329; -.
DR CTD; 1781; -.
DR eggNOG; KOG1587; Eukaryota.
DR InParanoid; Q0III3; -.
DR OrthoDB; 1453532at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..612
FT /note="Cytoplasmic dynein 1 intermediate chain 2"
FT /id="PRO_0000277462"
FT REPEAT 251..300
FT /note="WD 1"
FT REPEAT 304..344
FT /note="WD 2"
FT REPEAT 353..394
FT /note="WD 3"
FT REPEAT 403..443
FT /note="WD 4"
FT REPEAT 448..493
FT /note="WD 5"
FT REPEAT 496..536
FT /note="WD 6"
FT REPEAT 542..581
FT /note="WD 7"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 51
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88487"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
SQ SEQUENCE 612 AA; 68377 MW; 5CE1B00785190A4E CRC64;
MSDKSELKAE LERKKQRLAQ IREGKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA
EALLQSMGLT AESPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV
DFPPREIVTY TKETQTPVMA QPKEDEEEED DVVTPKPPIE PEEEKTLKKD EESDSKAPPH
ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS
LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEDAP HEPDGVALVW NMKYKKTTPE
YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC
VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN
FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHS AVGAVDFSHL FVTSSFDWTV
KLWTTKNNKP LYSFEDNSDY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS
VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP RNDEWARFGR TLAEINANRA
DAEEEAATRI PA
